Septin-12

Intramolecular

A redox-regulated disulphide may form within Septin-12 between cysteines 160 and 161. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

6mqk

Structure name

crystal structure of gtpase domain of human septin 12 in complex with gdp

Structure deposition date

2018-10-10

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide accession

Q8IYM1

Residue number A

160

Residue number B

161

Peptide name

Septin-12

Ligandability

Cysteine 160 of Septin-12

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 161 of Septin-12

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Septin-12 between cysteines 161 and 184. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

6mq9

Structure name

crystal structure of gtpase domain of human septin 12 in complex with gmppnp

Structure deposition date

2018-10-09

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q8IYM1

Residue number A

161

Residue number B

184

Peptide name

Septin-12

Ligandability

Cysteine 161 of Septin-12

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 184 of Septin-12

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Septin-12 between cysteines 160 and 184. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?